1su4

Crystal structure of calcium ATPase with two bound calcium ions

spinqualitylabelsall models 1su4, resolution 2.40Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1su4 is a 1 chain structure with sequence from Oryctolagus cuniculus. This structure supersedes the now removed PDB entry 1eul. The March 2004 RCSB PDB Molecule of the Month feature on The Calcium Pump by David S. Goodsell is 10.2210/rcsb_pdb/mom_2004_3. The October 2009 RCSB PDB Molecule of the Month feature on Sodium-Potassium Pump by David Goodsell is 10.2210/rcsb_pdb/mom_2009_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, NA Related: 1iwo, 1vfp Activity: Calcium-transporting ATPase, with EC number 3.6.3.8 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [AT2A1_RABIT] This magnesium-dependent enzyme catalyzes the hydrolysis of ATP coupled with the translocation of calcium from the cytosol to the sarcoplasmic reticulum lumen. Contributes to calcium sequestration involved in muscular excitation/contraction (By similarity). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Calcium ATPase is a member of the P-type ATPases that transport ions across the membrane against a concentration gradient. Here we have solved the crystal structure of the calcium ATPase of skeletal muscle sarcoplasmic reticulum (SERCA1a) at 2.6 A resolution with two calcium ions bound in the transmembrane domain, which comprises ten alpha-helices. The two calcium ions are located side by side and are surrounded by four transmembrane helices, two of which are unwound for efficient coordination geometry. The cytoplasmic region consists of three well separated domains, with the phosphorylation site in the central catalytic domain and the adenosine-binding site on another domain. The phosphorylation domain has the same fold as haloacid dehalogenase. Comparison with a low-resolution electron density map of the enzyme in the absence of calcium and with biochemical data suggests that large domain movements take place during active transport. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 A resolution.,Toyoshima C, Nakasako M, Nomura H, Ogawa H Nature. 2000 Jun 8;405(6787):647-55. PMID:10864315 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also ATPase

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